Solution scattering suggests cross-linking function of telethonin in the complex with titin

TY - JOUR

T1 - Solution scattering suggests cross-linking function of telethonin in the complex with titin

AU - Zou, P J

AU - Gautel, M

AU - Geerlof, A

AU - Wilmanns, M

AU - Koch, M H J

AU - Svergun, D I

PY - 2003/1/24

Y1 - 2003/1/24

N2 - Telethonin interacts specifically with the two Z-disk IG-like domains (Z1Z2) at the N terminus of titin, the largest presently known protein. Analytical ultracentrifugation and synchrotron radiation x-ray scattering were employed to study the solution structures of Z1Z2 and its complexes with telethonin, and low resolution models were constructed ab initio from the scattering data. A seven residues-long polyhistidine tag was localized at the tip of the Z1 domain by comparison of independent models of native and His-tagged versions of Z1Z2. The stoichiometry and shape of the complex between the telethonin construct lacking the C terminus and Z1Z2 indicate antiparallel association of two Z1Z2 molecules with telethonin acting as a central linker. The complex of full-length telethonin with Z1Z2 appears to also have a 1:2 stoichiometry at concentrations below 1 mg/ml but dimerizes at higher concentrations. These results suggest a possible role of telethonin in linking titin filaments at the Z-disk periphery.

AB - Telethonin interacts specifically with the two Z-disk IG-like domains (Z1Z2) at the N terminus of titin, the largest presently known protein. Analytical ultracentrifugation and synchrotron radiation x-ray scattering were employed to study the solution structures of Z1Z2 and its complexes with telethonin, and low resolution models were constructed ab initio from the scattering data. A seven residues-long polyhistidine tag was localized at the tip of the Z1 domain by comparison of independent models of native and His-tagged versions of Z1Z2. The stoichiometry and shape of the complex between the telethonin construct lacking the C terminus and Z1Z2 indicate antiparallel association of two Z1Z2 molecules with telethonin acting as a central linker. The complex of full-length telethonin with Z1Z2 appears to also have a 1:2 stoichiometry at concentrations below 1 mg/ml but dimerizes at higher concentrations. These results suggest a possible role of telethonin in linking titin filaments at the Z-disk periphery.

UR - http://www.scopus.com/inward/record.url?scp=0037462655&partnerID=8YFLogxK

U2 - 10.1074/jbc.M210217200

DO - 10.1074/jbc.M210217200

M3 - Article

SN - 1083-351X

VL - 278

SP - 2636

EP - 2644

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 4

ER -